BMRB Entry 19507

Name: Backbone assignment and Secondary Structure of Intrinsically Unstructured Culture Filtrate Antigen protein (CFP10) from Mycobacterium Tuberculosis
Published: 2013-11-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19507

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone assignment and Secondary Structure of Intrinsically Unstructured Culture Filtrate Antigen protein (CFP10) from Mycobacterium Tuberculosis

Deposition date:

2013-09-19

Original release date:

2013-11-11

Authors:

Pandey, Himanshu; Guleria, Anupam; Raikwal, Nisha; Arora, Ashish; Kumar, Dinesh

Citation:

Citation: Guleria, Anupam; Raikwal, Nisha; Shukla, Vaibhav; Pandey, Himanshu; Arora, Ashish; Kumar, Dinesh. "Pseudo 5D HN(C)N Experiment to Facilitate the Assignment of Backbone Resonances in Proteins Exhibiting High Backbone Shift Degeneracy" .

Assembly members:

Assembly members:
CFP10, polymer, 113 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CFP10: MAEMKTDAATLAQEAGNFER ISGDLKTQIDQVESTAGSLQ GQWRGAAGTAAQAAVVRFQE AANKQKQELDEISTNIRQAG VQYSRADEEQQQALSSQMGF KLAAALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	317
15N chemical shifts	109
1H chemical shifts	109

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CFP10 Monomer	1

Entities:

Entity 1, CFP10 Monomer 113 residues - Formula weight is not available

1

MET

ALA

GLU

MET

LYS

THR

ASP

ALA

THR

2

LEU

ALA

GLN

GLU

ALA

GLY

ASN

PHE

GLU

ARG

3

ILE

SER

GLY

ASP

LEU

LYS

THR

GLN

ILE

ASP

4

GLN

VAL

GLU

SER

THR

ALA

GLY

SER

LEU

GLN

5

GLY

GLN

TRP

ARG

GLY

ALA

GLY

THR

ALA

6

ALA

GLN

ALA

VAL

ARG

PHE

GLN

GLU

7

ALA

ASN

LYS

GLN

LYS

GLN

GLU

LEU

ASP

8

GLU

ILE

SER

THR

ASN

ILE

ARG

GLN

ALA

GLY

9

VAL

GLN

TYR

SER

ARG

ALA

ASP

GLU

GLN

10

GLN

ALA

LEU

SER

GLN

MET

GLY

PHE

11

LYS

LEU

ALA

LEU

GLU

HIS

12

HIS

Samples:

sample_1: CFP10, [U-13C; U-15N], 0.8 – 1.0 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 290 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D hNCAnH	sample_1	isotropic	sample_conditions_1
reduced dimensionality (4,3)-hnCOCANH	sample_1	isotropic	sample_conditions_1
Pseudo 5D HN(C)N	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 800 MHz

PDB	1WA8 3FAV
DBJ	BAL68012 BAQ08111 GAA43756
EMBL	CCC28957 CCC46227 CCE39297 CCG13791 CCK53890
GB	AAC83445 AAK48356 AAL14999 ABQ75702 ABR08234
REF	NP_218391 NP_857541 WP_003399940 WP_003900771 WP_009937166
SP	P0A567 P9WNK4 P9WNK5
AlphaFold	P0A567 P9WNK4 P9WNK5